重组蛋白融合信号肽在大肠杆菌周质空间表达的研究进展

Advances in expression of recombinant protein fusion signal peptide in Escherichia coli

摘要:

重组蛋白在大肠杆菌中表达时，往往面临着形成包涵体的问题，而重组蛋白若是分泌至周质空间则基本解决了这一问题，周质空间的周质蛋白不仅能帮助重组蛋白正确折叠还有利于二硫键的生成。信号肽是一段由15-30个氨基酸组成，被融合在重组蛋白N端的短肽，按照结构、功能的不同可以划分为N区、H区和C区，具有引导重组蛋白转运至细胞周质空间的作用。本文综述了信号肽的结构组成、作用机理和基本分泌途径，讨论了信号肽的高效转运和筛选方法，总结了在大肠杆菌中重组蛋白融合信号肽实现周质表达的新进展，并对未来高效信号肽选择方面的研究进行了探讨。

Abstract:

A signal peptide is a short peptide fused in the recombinant protein N-terminus, generally composed of 15-30 amino acids, guiding the transport of recombinant protein to the periplasmic space of the cell. It is divided into N region, H region and C according to the structure and function. Recombined protein expression in Escherichia coli, often faces with the problem of forming an inclusion body. If the recombined protein is secreted into the periplasmic space, the periplasmic protein can not only help the recombination protein fold into to correct structure but also facilitate the production of disulfide bonds. This paper summarizes the structure composition, action structure and basic secretion pathways of signal peptides; discusses the efficient transport and screening methods of signal peptides. This paper also summarizes the new progress of recombination protein fusion signal peptides in E. coli to achieve perennial expression, and visions the screening techniques of signal peptides in the future.